Mechanism of insect resistance to the microbial insecticide Bacillus thuringiensis.
Receptor binding studies show that resistance of a laboratory-selected Plodia interpunctella strain to a Bacillus thuringiensis insecticidal crystal protein (ICP) is correlated with a 50-fold reduction in affinity of the membrane receptor for this protein. The strain is sensitive to a second type of ICP that apparently recognizes a different receptor. Understanding the mechanism of resistance will provide strategies to prevent or delay resistance and hence prolong the usefulness of B. thuringiensis ICPs as environmentally safe insecticides.
Van Rie
J
J
Plant Genetic Systems, Gent, Belgium.
McGaughey
W H
WH
Johnson
D E
DE
Barnett
B D
BD
Van Mellaert
H
H
D000818:Animals; D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism; D001427:Bacterial Toxins / Q000378:metabolism; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D004731:Endotoxins; D006460:Hemolysin Proteins; D007305:Insecticide Resistance / Q000502:physiology*; D007915:Lepidoptera; D008871:Microvilli / Q000378:metabolism; D009036:Moths; D010572:Pest Control, Biological; D011955:Receptors, Drug / Q000378:metabolism
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011955:Receptors, Drug; C030956:insecticidal crystal protein, Bacillus Thuringiensis